N-(long-chain-acyl)ethanolamine deacylase

Last updated
N-(long-chain-acyl)ethanolamine deacylase
Identifiers
EC no. 3.5.1.60
CAS no. 99283-61-1
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

In enzymology, a N-(long-chain-acyl)ethanolamine deacylase (EC 3.5.1.60) is an enzyme that catalyzes the chemical reaction

N-(long-chain-acyl)ethanolamine + H2O a long-chain carboxylate + ethanolamine

Thus, the two substrates of this enzyme are N-(long-chain-acyl)ethanolamine and H2O, whereas its two products are long-chain carboxylate and ethanolamine.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-(long-chain-acyl)ethanolamine amidohydrolase. Other names in common use include N-acylethanolamine amidohydrolase, and acylethanolamine amidase.

Related Research Articles

<span class="mw-page-title-main">Carboxylic acid</span> Organic compound containing a –C(=O)OH group

In organic chemistry, a carboxylic acid is an organic acid that contains a carboxyl group attached to an R-group. The general formula of a carboxylic acid is R−COOH or R−CO2H, with R referring to the alkyl, alkenyl, aryl, or other group. Carboxylic acids occur widely. Important examples include the amino acids and fatty acids. Deprotonation of a carboxylic acid gives a carboxylate anion.

The enzyme acyl-CoA hydrolase (EC 3.1.2.20) catalyzes the reaction

The enzyme ADP-dependent medium-chain-acyl-CoA hydrolase (EC 3.1.2.19) catalyzes the reaction

The enzyme ADP-dependent short-chain-acyl-CoA hydrolase (EC 3.1.2.18) catalyzes the reaction

The enzyme wax-ester hydrolase (EC 3.1.1.50) catalyzes the reaction

In enzymology, a 5-oxoprolinase (ATP-hydrolysing) (EC 3.5.2.9) is an enzyme that catalyzes the chemical reaction

In enzymology, an acyl-lysine deacylase (EC 3.5.1.17) is an enzyme that catalyzes the chemical reaction

In enzymology, an allophanate hydrolase (EC 3.5.1.54) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Amidase</span>

In enzymology, an amidase (EC 3.5.1.4, acylamidase, acylase (misleading), amidohydrolase (ambiguous), deaminase (ambiguous), fatty acylamidase, N-acetylaminohydrolase (ambiguous)) is an enzyme that catalyzes the hydrolysis of an amide. In this way, the two substrates of this enzyme are an amide and H2O, whereas its two products are monocarboxylate and NH3.

In enzymology, an aminoacylase (EC 3.5.1.14) is an enzyme that catalyzes the chemical reaction

In enzymology, an aryl-acylamidase (EC 3.5.1.13) is an enzyme that catalyzes the chemical reaction

In enzymology, a hydroxyisourate hydrolase (EC 3.5.2.17) is an enzyme that catalyzes the chemical reaction

In enzymology, a long-chain-fatty-acyl-glutamate deacylase (EC 3.5.1.55) is an enzyme that catalyzes the chemical reaction

In enzymology, a N-acyl-D-amino-acid deacylase (EC 3.5.1.81) is an enzyme that catalyzes the chemical reaction

In enzymology, a N-acyl-D-aspartate deacylase (EC 3.5.1.83) is an enzyme that catalyzes the chemical reaction

In enzymology, a N-acyl-D-glutamate deacylase (EC 3.5.1.82) is an enzyme that catalyzes the chemical reaction

In enzymology, a N-carbamoyl-L-amino-acid hydrolase (EC 3.5.1.87) is an enzyme that catalyzes the chemical reaction

In enzymology, a penicillin amidase (EC 3.5.1.11) is an enzyme that catalyzes the chemical reaction

Acyl-homoserine-lactone acylase (EC 3.5.1.97, acyl-homoserine lactone acylase, AHL-acylase, AiiD, N-acyl-homoserine lactone acylase, PA2385 protein, quorum-quenching AHL acylase, quorum-quenching enzyme, PvdQ, QuiP) is an enzyme with systematic name N-acyl-L-homoserine-lactone amidohydrolase. This enzyme functions as a quorum quencher by catalysing the following chemical reaction

N-acylethanolamine acid amide hydrolase (NAAA) EC 3.5.1.- is a member of the choloylglycine hydrolase family, a subset of the N-terminal nucleophile hydrolase superfamily. NAAA has a molecular weight of 31 kDa. The activation and inhibition of its catalytic site is of medical interest as a potential treatment for obesity and chronic pain. While it was discovered within the last decade, its structural similarity to the more familiar acid ceramidase (AC) and functional similarity to fatty acid amide hydrolase (FAAH) allow it to be studied extensively.

References